Scislowski P W, Pickard K
Rowett Research Institute, Bucksburn, Aberdeen, Scotland.
Mol Cell Biochem. 1993 Dec 8;129(1):39-45. doi: 10.1007/BF00926574.
Enzymatic activities catalysing the inter-conversion of L-methionine and its oxy analogue 4-methylthio-2-oxobutyric acid (2,4-KMB) were detected in the liver, skeletal muscle and heart of the laboratory rat and of sheep. In both species the highest activity of methionine transamination was found in the liver and was located in the cytoplasm and mitochondria. We propose that physiological and nutritional role of the cytoplasmic methionine transamination is amination of 2,4 KMB and formation of L-methionine while in mitochondria the activity is responsible for disposal of excess methionine is oxidised through oxidative decarboxylation of 2,4 KMB.
在实验大鼠和绵羊的肝脏、骨骼肌及心脏中,检测到了催化L-蛋氨酸及其氧类似物4-甲硫基-2-氧代丁酸(2,4-KMB)相互转化的酶活性。在这两个物种中,蛋氨酸转氨作用的最高活性均在肝脏中被发现,且定位于细胞质和线粒体。我们提出,细胞质中蛋氨酸转氨作用的生理和营养作用是2,4-KMB的氨基化及L-蛋氨酸的形成,而在线粒体中,该活性负责通过2,4-KMB的氧化脱羧作用处理过量的蛋氨酸,使其被氧化。